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Authors = Maria Del Ben

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MARIA (3887) , DEL (1821) , BEN (487)

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Open AccessArticle Technological Implications of Modifying the Extent of Cell Wall-Proanthocyanidin Interactions Using Enzymes
Int. J. Mol. Sci. 2016, 17(1), 123; doi:10.3390/ijms17010123
Received: 16 December 2015 / Revised: 8 January 2016 / Accepted: 11 January 2016 / Published: 18 January 2016
Cited by 2 | Viewed by 903 | PDF Full-text (882 KB) | HTML Full-text | XML Full-text
Abstract
The transference and reactivity of proanthocyanidins is an important issue that affects the technological processing of some fruits, such as grapes and apples. These processes are affected by proanthocyanidins bound to cell wall polysaccharides, which are present in high concentrations during the processing
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The transference and reactivity of proanthocyanidins is an important issue that affects the technological processing of some fruits, such as grapes and apples. These processes are affected by proanthocyanidins bound to cell wall polysaccharides, which are present in high concentrations during the processing of the fruits. Therefore, the effective extraction of proanthocyanidins from fruits to their juices or derived products will depend on the ability to manage these associations, and, in this respect, enzymes that degrade these polysaccharides could play an important role. The main objective of this work was to test the role of pure hydrolytic enzymes (polygalacturonase and cellulose) and a commercial enzyme containing these two activities on the extent of proanthocyanidin-cell wall interactions. The results showed that the modification promoted by enzymes reduced the amount of proanthocyanidins adsorbed to cell walls since they contributed to the degradation and release of the cell wall polysaccharides, which diffused into the model solution. Some of these released polysaccharides also presented some reactivity towards the proanthocyanidins present in a model solution. Full article
(This article belongs to the Special Issue Phenolics and Polyphenolics 2015)
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Open AccessReview Does Lysosomial Acid Lipase Reduction Play a Role in Adult Non-Alcoholic Fatty Liver Disease?
Int. J. Mol. Sci. 2015, 16(12), 28014-28021; doi:10.3390/ijms161226085
Received: 13 October 2015 / Revised: 6 November 2015 / Accepted: 17 November 2015 / Published: 25 November 2015
Cited by 2 | Viewed by 1670 | PDF Full-text (456 KB) | HTML Full-text | XML Full-text
Abstract
Lysosomal Acid Lipase (LAL) is a key enzyme involved in lipid metabolism, responsible for hydrolysing the cholesteryl esters and triglycerides. Wolman Disease represents the early onset phenotype of LAL deficiency rapidly leading to death. Cholesterol Ester Storage Disease is a late onset phenotype
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Lysosomal Acid Lipase (LAL) is a key enzyme involved in lipid metabolism, responsible for hydrolysing the cholesteryl esters and triglycerides. Wolman Disease represents the early onset phenotype of LAL deficiency rapidly leading to death. Cholesterol Ester Storage Disease is a late onset phenotype that occurs with fatty liver, elevated aminotransferase levels, hepatomegaly and dyslipidaemia, the latter characterized by elevated LDL-C and low HDL-C. The natural history and the clinical manifestations of the LAL deficiency in adults are not well defined, and the diagnosis is often incidental. LAL deficiency has been suggested as an under-recognized cause of dyslipidaemia and fatty liver. Therefore, LAL activity may be reduced also in non-obese patients presenting non-alcoholic fatty liver disease (NAFLD), unexplained persistently elevated liver transaminases or with elevation in LDL cholesterol. In these patients, it could be indicated to test LAL activity. So far, very few studies have been performed to assess LAL activity in representative samples of normal subjects or patients with NAFLD. Moreover, no large study has been carried out in adult subjects with NAFLD or cryptogenic cirrhosis. Full article
(This article belongs to the Special Issue Non-Alcoholic Fatty Liver Disease Research 2016)

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